Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.10 extracted from

  • Xu, W.; Ni, D.; Yu, S.; Zhang, T.; Mu, W.
    Insights into hydrolysis versus transfructosylation Mutagenesis studies of a novel levansucrase from Brenneria sp. EniD312 (2018), Int. J. Biol. Macromol., 116, 335-345 .
    View publication on PubMed
Search for more literature for 2.4.1.10

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Brenneria sp. EniD312

Protein Variants

Protein Variants Comment Organism
A154S the mutant shows reduced activity compared to the wild type enzyme Brenneria sp. EniD312
D225A inactive Brenneria sp. EniD312
D268A inactive Brenneria sp. EniD312
E309A inactive Brenneria sp. EniD312
H327A the mutant shows reduced activity compared to the wild type enzyme Brenneria sp. EniD312
H327R the mutant shows reduced activity compared to the wild type enzyme Brenneria sp. EniD312

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside Brenneria sp. EniD312
-
 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?

Organism

Organism UniProt Comment Textmining
Brenneria sp. EniD312
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-chelating affinity chromatography and Superdex S200 gel filtration Brenneria sp. EniD312

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + sucrose
-
 Brenneria sp. EniD312 D-glucose + levan
-
 ?
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
-
 Brenneria sp. EniD312 D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
-
 ?

Subunits

Subunits Comment Organism
? x * 49000, SDS-PAGE Brenneria sp. EniD312
? x * 48530, calculated from amino acid sequence Brenneria sp. EniD312

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 transfructosylation activtiy Brenneria sp. EniD312
50
-
 hydrolytic activtiy Brenneria sp. EniD312

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35 55 the enzyme displays a reasonable thermostability at 35°C and remains near 60% of initial activity when incubated at 35°C for 3 h. However, the enzyme behaves weak thermostability at a higher temperature, which exhibits the half-life of 2 h at 45°C and 1.2 h at 55°C Brenneria sp. EniD312

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Brenneria sp. EniD312

pH Range

pH Minimum pH Maximum Comment Organism
6 8.5 the enzyme remains relative activity in the pH range of from 6.5 to 8.0. The enzyme retains more than 80% of initial activity when pH varying from 6.0 to 7.5 at 45°C, but loses almost 60% transfructosylation activity when the pH shifts to lower than 5.5 or higher than 8.0 Brenneria sp. EniD312

pI Value

Organism Comment pI Value Maximum pI Value
Brenneria sp. EniD312 calculated from amino acid sequence
-
 4.6